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PPR proteins shed a new light on RNase P biology.

ABSTRACT: A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset of PPR proteins called PRORP possesses RNase P activity in several eukaryotes, both in nuclei and organelles. RNase P is the endonucleolytic activity that removes 5' leader sequences from tRNA precursors and is thus essential for translation. Before the characterization of PRORP, RNase P enzymes were thought to occur universally as ribonucleoproteins, although some evidence implied that some eukaryotes or cellular compartments did not use RNA for RNase P activity. The characterization of PRORP reveals a two-domain enzyme, with an N-terminal domain containing multiple PPR motifs and assumed to achieve target specificity and a C-terminal domain holding catalytic activity. The nature of PRORP interactions with tRNAs suggests that ribonucleoprotein and protein-only RNase P enzymes share a similar substrate binding process.

SUBMITTER: Pinker F

PROVIDER: S-EPMC3858429 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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PPR proteins shed a new light on RNase P biology.

Pinker Franziska F Bonnard Géraldine G Gobert Anthony A Gutmann Bernard B Hammani Kamel K Sauter Claude C Gegenheimer Peter A PA Giegé Philippe P

RNA biology 20130619 9

A fast growing number of studies identify pentatricopeptide repeat (PPR) proteins as major players in gene expression processes. Among them, a subset of PPR proteins called PRORP possesses RNase P activity in several eukaryotes, both in nuclei and organelles. RNase P is the endonucleolytic activity that removes 5' leader sequences from tRNA precursors and is thus essential for translation. Before the characterization of PRORP, RNase P enzymes were thought to occur universally as ribonucleoprotei ...[more]

PMID: 23925311

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